http://purl.uniprot.org/citations/11472023 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11472023 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11472023 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
http://purl.uniprot.org/citations/11472023 | http://www.w3.org/2000/01/rdf-schema#comment | "Chlorite dismutase has been purified from the chlorate-metabolizing bacterium Ideonella dechloratans. The purified enzyme is tetrameric, with a relative molecular mass of 25,000 for the subunit, and contains about 0.6 heme/subunit as isolated. Its catalytic properties are similar, but not identical, to those found for a similar enzyme purified earlier from the bacterium GR-1. The heme group in Ideonella chlorite dismutase is readily reduced by dithionite, in contrast to the GR-1 enzyme, and redox titration gave a value of -21 mV for the midpoint potential at pH 7. The heme group has been characterized by optical and EPR spectroscopy. It is high-spin ferric at neutral pH, with spectroscopic properties similar to those found for cytochrome c peroxidase. In the alkaline pH range, a low-spin compound is formed. A 22-residue N-terminal amino acid sequence has been determined and no homologue has been found in the protein sequence databases."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.org/dc/terms/identifier | "doi:10.1007/s007750100237"xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.org/dc/terms/identifier | "doi:10.1007/s007750100237"xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Aasa R."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Aasa R."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Bergius H."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Bergius H."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Danielsson Thorell H."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Danielsson Thorell H."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Nilsson T."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Nilsson T."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Stenklo K."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/author | "Stenklo K."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/name | "J. Biol. Inorg. Chem."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/name | "J. Biol. Inorg. Chem."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/pages | "601-607"xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/pages | "601-607"xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/title | "Chlorite dismutase from Ideonella dechloratans."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/title | "Chlorite dismutase from Ideonella dechloratans."xsd:string |
http://purl.uniprot.org/citations/11472023 | http://purl.uniprot.org/core/volume | "6"xsd:string |